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meso -Diaminopimelate dehydrogenase (meso -DAPDH) is an NADP+ -dependent enzyme which catalyzes the reversible oxidative deamination on thed -configuration ofmeso -2,6-diaminopimelate to producel -2-amino-6-oxopimelate. In this study, the gene encoding ameso -diaminopimelate dehydrogenase fromSymbiobacterium thermophilum was cloned and expressed inEscherichia coli . In addition to the native substratemeso -2,6-diaminopimelate, the purified enzyme also showed activity towardd -alanine,d -valine, andd -lysine. This enzyme catalyzed the reductive amination of 2-keto acids such as pyruvic acid to generated -amino acids in up to 99% conversion and 99% enantiomeric excess. Sincemeso -diaminopimelate dehydrogenases are known to be specific tomeso -2,6-diaminopimelate, this is a unique wild-typemeso -diaminopimelate dehydrogenase with a more relaxed substrate specificity and potential ford -amino acid synthesis. The enzyme is the most stablemeso -diaminopimelate dehydrogenase reported to now. Two amino acid residues (F146 and M152) in the substrate binding sites ofS. thermophilum meso -DAPDH different from the sequences of other knownmeso -DAPDHs were replaced with the conserved amino acids in othermeso -DAPDHs, and assay of wild-type and mutant enzyme activities revealed that F146 and M152 are not critical in determining the enzyme's substrate specificity. The high thermostability and relaxed substrate profile ofS. thermophilum meso -DAPDH warrant it as an excellent starting enzyme for creating effectived -amino acid dehydrogenases by protein engineering.

applied and environmental microbiology

A Novel <i>meso</i> -Diaminopimelate Dehydrogenase from Symbiobacterium thermophilum: Overexpression, Characterization, and Potential for <scp>d</scp> -Amino Acid Synthesis

A Novel meso -Diaminopimelate Dehydrogenase from Symbiobacterium thermophilum: Overexpression, Characterization, and Potential for d -Amino Acid Synthesis